The structure and formation mechanism of blue-fluorescent lens proteins, which accumulate in the lens of the aging eye, will be explored. Blue-fluorescent lens proteins will be isolated from bovine lens by gel filtration or ion-exchange chromatography. The isolated proteins will then be characterized by visible and ultraviolet fluorescence, sedimentation, circular dichroism, gel electrophoresis, amino acid composition, chemical and other spectral studies. Production of blue-fluorescent lens proteins will also be carried out by irradiating whole lens samples as well as isolated non-blue-fluorescent proteins with near-ultraviolet light. The relationship between non-blue-fluorescent lens proteins alpha-, beta-, gamma- crystallins and albuminoid), native blue-fluorescent proteins and photochemically-producted blue-fluorescent proteins will be evaluated by investigating not only the aforementioned parameters, but their dissociation-association properties as well. The mercurial or urea-induced deaggregation of blue-fluorescent proteins, alpha- and beta-crystallins, as well as glucose or calcium ion-induced aggregation or reaggregation of blue-fluorescent proteins and alpha-crystallin, will be studied, again utilizing gel filtration, fluorescence, and circular dichroism as probes of the nature of aggregation interactions. Spin-labeling will be exploited as a method for probing the SH-group environment during deaggregation and aggregation.